Studies on inactivation and stabilization of manganese peroxidase from Trametes versicolor

被引:13
作者
Bermek, H [1 ]
Li, KC
Eriksson, KEL
机构
[1] Istanbul Tech Univ, Dept Mol Biol & Genet, TR-80626 Istanbul, Turkey
[2] Oregon State Univ, Dept Forest Prod, Corvallis, OR 97331 USA
[3] Univ Georgia, Dept Biochem & Mol Biol, Ctr Biol Resource Recovery, Athens, GA 30602 USA
来源
BIOTECHNOLOGY IN THE PULP AND PAPER INDUSTRY: 8TH ICBPPI | 2002年 / 21卷
关键词
D O I
10.1016/S0921-0423(02)80016-8
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
High concentrations of H2O2 cause inactivation of manganese peroxidase (MnP). The mechanism of this inactivation has been investigated. A method for stabilization of MnP used for pulp bleaching in the presence of high concentrations of H2O2 has been developed. It was demonstrated that formation of the inactive form of MnP (Compound III) is the major reason for the inactivation in which hydroxyl free radicals or superoxide anion radicals are not involved. It was also found that 1-hydroxybenzotriazole, 2,2,6,6-tetramethyl-1-piperidinyloxy free radical, violuric acid, 3-hydroxy-1,2,3-benzotriazin-4-(3H)-one and chlorpromazine stabilized MnP. The stabilizing effect by 1-hydroxybenzotriazole is due to the conversion of the inactive Compound III to the native enzyme.
引用
收藏
页码:141 / 149
页数:9
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